8F15
Structure of the STUB1 TPR domain in complex with H202, an all-D Helicon Polypeptide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL45XU |
| Synchrotron site | SPring-8 |
| Beamline | BL45XU |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2022-02-06 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 1.0000 |
| Spacegroup name | P 43 |
| Unit cell lengths | 50.560, 50.560, 199.850 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 49.020 - 1.730 |
| Rwork | 0.180 |
| R-free | 0.20960 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3q49 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.18.2) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 49.020 | 1.760 |
| High resolution limit [Å] | 1.730 | 1.730 |
| Rmerge | 0.102 | 1.240 |
| Number of reflections | 51998 | 2848 |
| <I/σ(I)> | 16.6 | 2.2 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 13.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 291 | 0.1 M TRIS pH 8, 30% v/v PEG 400 |
